PMID: 9738007

Gasparini S, Danse JM, Lecoq A, Pinkasfeld S, Zinn-Justin S, Young LC, de Medeiros CC, Rowan EG, Harvey AL, Menez A
Delineation of the functional site of alpha-dendrotoxin. The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channel-blocking toxins.
J Biol Chem. 1998 Sep 25;273(39):25393-403., [PubMed]
Sentences
No. Mutations Sentence Comment
134 ABCC8 p.Asp18Ala
X
ABCC8 p.Asp18Ala 9738007:134:58
status: NEW
view ABCC8 p.Asp18Ala details
 The other substitutions (P2A, H10A, R11A, R15A, Y17A, and D18A) and the previously described mutation D12N (32) did not significantly reduce the affinity. Login to comment 193 ABCC8 p.Asp18Ala
X
ABCC8 p.Asp18Ala 9738007:193:800
status: NEW
view ABCC8 p.Asp18Ala details
 The spectra were recorded at 20 °C in 0.1-cm cuvettes, with a protein concentration of 5-10 ␮M. TABLE I Affinity of ␣DTX analogs determined by their ability to compete with [125 I]␣DTX for binding to rat brain synaptosomal membranes ␣DTX Ki a Ki analog/Ki WTb pM WT 4 Ϯ 1 1 P2A 10.6 Ϯ 1.1 2.9 Ϯ 1.0 R3A 28.5 Ϯ 4.6 7.9 Ϯ 3.1 R4A 38 Ϯ 12 11 Ϯ 5.75 K5A 5800 Ϯ 700 1594 Ϯ 574 K5Orn 471 Ϯ 42 128 Ϯ 43 K5Nle 5700 Ϯ 400 1547 Ϯ 487 L6A 43.4 Ϯ 12 12.4 Ϯ 6.1 I8A 118 Ϯ 26 33.2 Ϯ 14.8 L9A 4160 Ϯ 900 1170 Ϯ 518 H10A 1.6 Ϯ 0.2 0.45 Ϯ 0.15 R11A 3.0 Ϯ 0.1 0.8 Ϯ 0.2 R15A 4.6 Ϯ 0.1 1.22 Ϯ 0.33 Y17A 3.7 Ϯ 0.1 1.0 Ϯ 0.27 D18A 3.4 Ϯ 0.1 0.91 Ϯ 0.25 K19A 2.3 Ϯ 0.1 0.63 Ϯ 0.17 Q27A 2.9 Ϯ 0.1 0.78 Ϯ 0.21 Q31A 3.65 Ϯ 0.05 0.98 Ϯ 0.26 E33A 5.3 Ϯ 0.05 1.42 Ϯ 0.37 R34A 7.1 Ϯ 0.1 1.9 Ϯ 0.5 D36A 4.85 Ϯ 0.1 1.30 Ϯ 0.35 S38A 23.5 Ϯ 6.5 6.64 Ϯ 3.24 S44A 6.7 Ϯ 0.1 1.8 Ϯ 0.45 R46A 562 Ϯ 152 160 Ϯ 78 K48A 2.8 Ϯ 0.05 0.75 Ϯ 0.2 E51A 3.65 Ϯ 0.05 0.98 Ϯ 0.26 R54A 5.4 Ϯ 0.05 1.44 Ϯ 0.38 R55A 4.0 Ϯ 0.21 1.08 Ϯ 0.3 I58A 3.45 Ϯ 0.25 1.27 Ϯ 0.63 a Ki Ϯ S.E. values are calculated from competition experiments as described in the legend of Fig. 5. b WT, wild type. Login to comment